Frank Schumer

Voltammetric and spectroelectrochemical studies on 4-aminophenol at gold electrodes in aqueous and organic media

Abstract Voltammetric and UV–Vis spectroelectrochemical studies on 4-aminophenol (4-AP) at gold electrodes have been carried out in conventional electrochemical and in novel spectroelectrochemical cells. As base electrolytes acetonitrile with 10−2 M tetrabutylammonium hexafluorophosphate as supporting electrolyte and acetate buffer (pH 4.6) solutions have been used. 4-AP was electrochemically oxidized at gold electrodes at potentials >+0.1 V in aqueous solutions and at potentials >+0.5 V in acetonitrile solutions. The formation of an oxidation product has been characterized in situ by UV–Vis spectroscopy in a novel optical thin-layer spectroelectrochemical cell.

Highly sensitive protein detection based on lanthanide chelates with antenna ligands providing a linear range of five orders of magnitude.

Protein detection is an important task for pharmaceutical and clinical research today. Numerous protein staining techniques exist but are limited regarding their sensitivity and often narrow linear quantification ranges. To the best of our knowledge, this is the first description of a novel class of lanthanide chelatators, which absorb in the lower energy region at 360 nm. The new compound (6,9-dicarboxymethyl-3-{4-([1,10]-phenanthrol-2-ylethinylphenyl-carbamoyl)-methyl}-3,6,9-triaza-)-undeca-1,11-dicarboxylic acid) was coupled to different proteins and showed highly sensitive protein detection limits in both sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) (1.5 fmol of bovine serum albumin) as well as Dot Blot (100 amol of lysozyme). Furthermore, the novel compound shows an exceptionally broad linear quantification range over 5 orders of magnitude allowing applications that require the highest sensitivity alongside standard sensitivity. In addition, the new compound offers multiplexing capabilities.

Isoserine-based biotinylated photoaffinity probes that interact with penicillin-binding protein 1bElectronic supplementary information (ESI) available: spectroscopic characterization for all new compounds. Fig. S1: decrease in absorbance at 366 nm as a function of irradiation time for 1b. See http://www.rsc.org/suppdata/cc/b2/b204007g/

The photolytic decomposition of trifunctional carbene generating photoaffinity probes in methanolic solution was studied, a cleavage reaction with butylamine in water, the conjugation with a ligand (moenomycin), and experiments that demonstrate that the fully armed probes interact with penicillin-binding protein 1b.